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From Proteopedia
YODA FROM ESCHERICHIA COLI CRYSTALLISED WITH ZINC IONS
Structural highlights
Function[YODA_ECOLI] May function as a periplasmic zinc chaperone or mediate direct transport of zinc from the periplasm to the cytoplasm under zinc-limited conditions. Binds zinc with high affinity, and can also bind cadmium, mercury or nickel. Preferentially binds Zn(2+) over Cd(2+). Contains one high affinity metal binding site, and can bind additional metal ions at other sites.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have determined the crystal structure of YodA, an Escherichia coli protein of unknown function. YodA had been identified under conditions of cadmium stress, and we confirm that it binds metals such as cadmium and zinc. We have also found nickel bound in one of the crystal forms. YodA is composed of two domains: a main lipocalin/calycin-like domain and a helical domain. The principal metal-binding site lies on one side of the calycin domain, thus making YodA the first metal-binding lipocalin known. Our experiments suggest that YodA expression may be part of a more general stress response. From sequence analogy with the C-terminal domain of a metal-binding receptor of a member of bacterial ATP-binding cassette transporters, we propose a three-dimensional model for this receptor and suggest that YodA may have a receptor-type partner in E. coli. YodA from Escherichia coli is a metal-binding, lipocalin-like protein.,David G, Blondeau K, Schiltz M, Penel S, Lewit-Bentley A J Biol Chem. 2003 Oct 31;278(44):43728-35. Epub 2003 Aug 8. PMID:12909634[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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